ArticlePLoS pathogens2012
Propagation of RML prions in mice expressing PrP devoid of GPI anchor leads to formation of a novel, stable prion strain.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 32 citations in OpenAlex.
- Partial Deletion of the Carboxyl-Terminal Signal Sequence of the Cellular Prion Protein Alters Protein Expression via Endoplasmic Reticulum-Associated Degradation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- A Comparison of RML Prion Inactivation Efficiency by Heterogeneous and Homogeneous Photocatalysis.Pathogens (Basel, Switzerland) · 2024Article
- Prion assemblies: structural heterogeneity, mechanisms of formation, and role in species barrier.Cell and tissue research · 2023Review
- Structural biology of ex vivo mammalian prions.The Journal of biological chemistry · 2022Review
- Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains.Nature communications · 2022Article
- Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.Molecules (Basel, Switzerland) · 2022Review
- Cofactor and glycosylation preferences for in vitro prion conversion are predominantly determined by strain conformation.PLoS pathogens · 2020Article
- Full restoration of specific infectivity and strain properties from pure mammalian prion protein.PLoS pathogens · 2019Article
- Preserving prion strain identity upon replication of prions in vitro using recombinant prion protein.Acta neuropathologica communications · 2018Article
- Article
- Post-translational modifications in PrP expand the conformational diversity of prions in vivo.Scientific reports · 2017Article
- Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio.Scientific reports · 2015Article
- Two alternative pathways for generating transmissible prion disease de novo.Acta neuropathologica communications · 2015Article
- Increased infectivity of anchorless mouse scrapie prions in transgenic mice overexpressing human prion protein.Journal of virology · 2015Article
- Review
- Article
- Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion.Journal of virology · 2014Article
- Liberation of GPI-anchored prion from phospholipids accelerates amyloidogenic conversion.International journal of molecular sciences · 2013Article
- Probing early misfolding events in prion protein mutants by NMR spectroscopy.Molecules (Basel, Switzerland) · 2013Review
- Acquisition of drug resistance and dependence by prions.PLoS pathogens · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
PrP(C), a host protein which in prion-infected animals is converted to PrP(Sc), is linked to the cell membrane by a GPI anchor. Mice expressing PrP(C) without GPI anchor (tgGPI⁻ mice), are susceptible to prion infection but accumulate anchorless PrP(Sc) extra-, rather than intracellularly. We investigated whether tgGPI⁻ mice could faithfully propagate prion strains despite the deviant structure and location of anchorless PrP(Sc). We found that RML and ME7, but not 22L prions propagated in tgGPI⁻ brain developed novel cell tropisms, as determined by the Cell Panel Assay (CPA). Surprisingly, the levels of proteinase K-resistant PrP(Sc) (PrP(res)) in RML- or ME7-infected tgGPI⁻ brain were 25-50 times higher than in wild-type brain. When returned to wild-type brain, ME7 prions recovered their original properties, however RML prions had given rise to a novel prion strain, designated SFL, which remained unchanged even after three passages in wild-type mice. Because both RML PrP(Sc) and SFL PrP(Sc) are stably propagated in wild-type mice we propose that the two conformations are separated by a high activation energy barrier which is abrogated in tgGPI⁻ mice.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.